Fatty acid transport protein 1 and long-chain acyl coenzyme A synthetase 1 interact in adipocytes
Fatty acid transport protein 1 and long-chain acyl coenzyme A synthetase 1 interact in adipocytes
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DOI：
10.1194/jlr.m500514-jlr200
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发表时间：
2006-03-01
影响因子：
6.5
通讯作者：
Schaffer, JE
中科院分区：
文献类型：
--
作者：
Richards, MR;Harp, JD;Schaffer, JE
脂肪酸转运蛋白（FATP）和长链酰基辅酶A合成酶（ACSL）蛋白已被证明在生理条件下促进哺乳动物细胞中的长链脂肪酸（LCFA）转运中起作用。FATP和ACSL蛋白的参与与矢量酰化模型一致，其中脂肪酸转运与酯化反应偶联。本研究旨在确定这些蛋白质的功能是否通过蛋白质-蛋白质相互作用协调，这种相互作用可能作为细胞脂肪酸转运的调节点。我们首次证明了FATP 1和ACSL 1在3 T3-L1脂肪细胞中共免疫沉淀，表明这些蛋白质形成寡聚复合物。急性胰岛素治疗（刺激脂肪酸摄取）或异丙肾上腺素治疗（减少脂肪酸摄取并刺激脂解）均未改变FATP 1和ACSL 1免疫共沉淀的效率。此外，抑制脂肪细胞中的ACSL 1活性会损害脂肪酸摄取，这表明酯化对于脂肪酸转运至关重要。总之，我们的研究结果表明，FATP 1和ACSL 1之间的组成性相互作用有助于通过载体酰化在脂肪细胞中有效的细胞摄取LCFA。
The fatty acid transport proteins ( FATP) and long-chain acyl coenzyme A synthetase (ACSL) proteins have been shown to play a role in facilitating long-chain fatty acid (LCFA) transport in mammalian cells under physiologic conditions. The involvement of both FATP and ACSL proteins is consistent with the model of vectorial acylation, in which fatty acid transport is coupled to esterification. This study was undertaken to determine whether the functions of these proteins are coordinated through a protein-protein interaction that might serve as a point of regulation for cellular fatty acid transport. We demonstrate for the first time that FATP1 and ACSL1 coimmunoprecipitate in 3T3-L1 adipocytes, indicating that these proteins form an oligomeric complex. The efficiency of FATP1 and ACSL1 coimmunoprecipitation is unaltered by acute insulin treatment, which stimulates fatty acid uptake, or by treatment with isoproterenol, which decreases fatty acid uptake and stimulates lipolysis. Moreover, inhibition of ACSL1 activity in adipocytes impairs fatty acid uptake, suggesting that esterification is essential for fatty acid transport. Together, our findings suggest that a constitutive interaction between FATP1 and ACSL1 contributes to the efficient cellular uptake of LCFAs in adipocytes through vectorial acylation.